A CLC-type F^-/H⁺ antiporter in ion-swapped conformations.

ABSTRACT: Fluoride/proton antiporters of the CLC^F family combat F^- toxicity in bacteria by exporting this halide from the cytoplasm. These transporters belong to the widespread CLC superfamily but display transport properties different from those of the well-studied Cl^-/H⁺ antiporters. Here, we report a structural and functional investigation of these F^--transport proteins. Crystal structures of a CLC^F homolog from Enterococcus casseliflavus are captured in two conformations with simultaneous accessibility of F^- and H⁺ ions via separate pathways on opposite sides of the membrane. Manipulation of a key glutamate residue critical for H⁺ and F^- transport reverses the anion selectivity of transp

SUBMITTER: Last NB 

PROVIDER: S-EPMC6044475 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature